Work in this laboratory has been focused on the determination of three- dimensional structures of larger proteins in solution by NMR, with a particular emphasis on protein-protein, protein-ligand and protein-DNA complexes. A considerable effort has been placed on the development of three- and four-dimensional heteronuclear NMR to extend the application of NMR as a method for determining three-dimensional structures of proteins in solution beyond the limits of conventional two-dimensional NMR (-100 residues) to molecules in the 150- to 400- residue range, and to develop new NMR methods for determining long range order apriori, including the dependence of heteronuclear relexation data on diffusion anisotropy and the use of residual dipolar couplings. Solution structures of a number of proteins have been determined. These include the complexes of the transcription factors GAGA, AreA and HMG-I/Y with DNA, the DNA MuA binding domains of the Mu transposase, the 30 kDa (259 residue) N terminal domain of Enzyme I of the PTS pathway, the 40 kDa complex of the N-terminal domain of enzyme I with the histidine containing protein HPr (40 kDa),the complete 44 kDa trimeric ectodomain of gp41, theN-terminal domain of HIV-1 integrase, and the barrier-to- autointegration factor BAF. - Structural Biology / Proteins / Solution Structure / NMR / protein-DNA complexes / protein-protein complexes